|
Name |
Accession |
Description |
Interval |
E-value |
| V-ATPase_V1_A |
TIGR01042 |
V-type (H+)-ATPase V1, A subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
20-612 |
0e+00 |
|
V-type (H+)-ATPase V1, A subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273411 [Multi-domain] Cd Length: 591 Bit Score: 1266.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 20 ECGYVRKVSGPVVIADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILG 99
Cdd:TIGR01042 1 EYGYIYKVSGPVVVAENMAGAAMYELVRVGHDELVGEIIRLEGDKATIQVYEETSGLTVGDPVLRTGKPLSVELGPGILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 100 NIFDGIQRPLKTIAKRSGDVYIPRGVSVPALDKDILWEFQPKKKGEGDLITGGDLYATVFENSLVEHHIALPPDAMGKIT 179
Cdd:TIGR01042 81 NIFDGIQRPLKAIAEQSQSIYIPRGVNVPALDRDKKWEFTPKKLRVGDHITGGDIYGTVFENSLIKHKIMLPPRARGTIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 180 YIAPPGQYSLKDTVLELEFQGVKKKFTMLQTWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKT 259
Cdd:TIGR01042 161 YIAPAGNYTVDDTVLEVEFQGVKKKFSMLQTWPVRSPRPVTEKLPANTPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 260 VISQALSKYSNSDTVVYVGCGERGNEMAEVLMDFPQLTMTLpDGREESVMKRTTLVANTSNMPVAAREASIYTGITIAEY 339
Cdd:TIGR01042 241 VISQSLSKYSNSDAIVYVGCGERGNEMAEVLMDFPELTMEV-DGREESIMKRTTLVANTSNMPVAAREASIYTGITLAEY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 340 FRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPERNGSVTIVGAVSPPGGD 419
Cdd:TIGR01042 320 FRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGSPEREGSVSIVGAVSPPGGD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 420 FSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALESFYEKFDSDFIDIRTKAREVLQREDDLNEIVQLV 499
Cdd:TIGR01042 400 FSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALEEFYEKFYPEFVPLRTKAKEILQEEEDLNEIVQLV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 500 GKDALAETDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERGAGmDGQKITYTLIKHRLG 579
Cdd:TIGR01042 480 GKDALAETDKITLEVAKLIKEDFLQQNGYTPYDRFCPFYKTVGMMRNMIAFYDLARQAVERTAQ-DDNKITWSIIKESLG 558
|
570 580 590
....*....|....*....|....*....|...
gi 976921132 580 DLFYRLVSQKFEDPAEGEDVLIGKFKKLNEDLS 612
Cdd:TIGR01042 559 DLLYRLSSMKFEDPSDGEAKIKADYEKLNEDMQ 591
|
|
| NtpA |
COG1155 |
Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]; ... |
22-618 |
0e+00 |
|
Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 440769 [Multi-domain] Cd Length: 583 Bit Score: 958.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 22 GYVRKVSGPVVIADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILGNI 101
Cdd:COG1155 5 GKIVKINGPLVTAEGMGGAKMYEVVYVGEERLIGEVIRIEGDKATIQVYEETSGLKPGEPVESTGEPLSVELGPGLLGNI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 102 FDGIQRPLKTIAKRSGDvYIPRGVSVPALDKDILWEFQPKKKgEGDLITGGDLYATVFENSLVEHHIALPPDAMGKITYI 181
Cdd:COG1155 85 FDGIQRPLDKIAEKSGD-FIPRGVDVPALDREKKWDFTPTVK-VGDKVSAGDILGTVQETPLIEHKIMVPPGVSGTVKEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 182 APPGQYSLKDTVLELE-FQGVKKKFTMLQTWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTV 260
Cdd:COG1155 163 APEGEYTVEDTIAVLEdEDGEEHELTMYQKWPVRRPRPYKEKLPPSEPLITGQRVIDTFFPIAKGGTAAIPGPFGTGKTV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 261 ISQALSKYSNSDTVVYVGCGERGNEMAEVLMDFPQLTmtlpD---GReeSVMKRTTLVANTSNMPVAAREASIYTGITIA 337
Cdd:COG1155 243 TQHQLAKWSDADIVVYVGCGERGNEMTEVLEEFPELI----DpktGR--PLMERTVLIANTSNMPVAAREASIYTGITIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 338 EYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPErnGSVTIVGAVSPPG 417
Cdd:COG1155 317 EYYRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEE--GSVTIIGAVSPPG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 418 GDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALESFYEK-FDSDFIDIRTKAREVLQREDDLNEIV 496
Cdd:COG1155 395 GDFSEPVTQNTLRIVKVFWALDASLAYARHYPAINWLTSYSLYLDDLAEWYDEnVDPDWSELRNEAMDLLQEEAELQEIV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 497 QLVGKDALAETDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERGAGMDgqkityTLIKH 576
Cdd:COG1155 475 RLVGEDALPDEDRLTLEVARLIREGFLQQNAFDDVDTYCPLEKQYKMLKLILTFYDKAFEALEKGVPLS------EIKEL 548
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 976921132 577 RLGDLFYRLvsqKFEDPAEGEDvligKFKKLNEDLSAGFRNL 618
Cdd:COG1155 549 PLREKIARM---KYSPENELLE----KFDELEKEIDEEIEEL 583
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
22-621 |
0e+00 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 910.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 22 GYVRKVSGPVVIADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILGNI 101
Cdd:PRK04192 5 GKIVRVSGPLVVAEGMGGARMYEVVRVGEEGLIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGEPLSVELGPGLLGSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 102 FDGIQRPLKTIAKRSGDvYIPRGVSVPALDKDILWEFQPKKKgEGDLITGGDLYATVFENSLVEHHIALPPDAMGKITYI 181
Cdd:PRK04192 85 FDGIQRPLDELAEKSGD-FLERGVYVPALDREKKWEFTPTVK-VGDKVEAGDILGTVQETPSIEHKIMVPPGVSGTVKEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 182 APPGQYSLKDTVLELE-FQGVKKKFTMLQTWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTV 260
Cdd:PRK04192 163 VSEGDYTVDDTIAVLEdEDGEGVELTMMQKWPVRRPRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 261 ISQALSKYSNSDTVVYVGCGERGNEMAEVLMDFPQLTmtlpD---GReeSVMKRTTLVANTSNMPVAAREASIYTGITIA 337
Cdd:PRK04192 243 TQHQLAKWADADIVIYVGCGERGNEMTEVLEEFPELI----DpktGR--PLMERTVLIANTSNMPVAAREASIYTGITIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 338 EYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPErnGSVTIVGAVSPPG 417
Cdd:PRK04192 317 EYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEE--GSVTIIGAVSPPG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 418 GDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALESFYEK-FDSDFIDIRTKAREVLQREDDLNEIV 496
Cdd:PRK04192 395 GDFSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYSLYLDQVAPWWEEnVDPDWRELRDEAMDLLQREAELQEIV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 497 QLVGKDALAETDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERGAGMDgqkityTLIKH 576
Cdd:PRK04192 475 RLVGPDALPEEDRLILEVARLIREDFLQQNAFDPVDTYCPPEKQYEMLKLILTFYDEAFKALEKGVPVS------EILEL 548
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 976921132 577 RLGDLFYRLvsqKFedpaEGEDVLIGKFKKLNEDLSAGFRNLEDE 621
Cdd:PRK04192 549 EVRDRIARL---KY----IPENEYLEKIDEIFEKLEEELEELIAE 586
|
|
| ATP_syn_A_arch |
TIGR01043 |
ATP synthase archaeal, A subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
22-616 |
0e+00 |
|
ATP synthase archaeal, A subunit; Archaeal ATP synthase shares extensive sequence similarity with eukaryotic and prokaryotic V-type (H+)-ATPases. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 130115 [Multi-domain] Cd Length: 578 Bit Score: 830.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 22 GYVRKVSGPVVIADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILGNI 101
Cdd:TIGR01043 2 GRIIRVSGPLVVADGMKGAQMYEVVKVGEEGLIGEIIRIEGDKAFIQVYEETSGIKPGEPVVGTGAPLSVELGPGLLGSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 102 FDGIQRPLKTIAKRSGDvYIPRGVSVPALDKDILWEFQPKKKgEGDLITGGDLYATVFENSLVEHHIALPPDAMGKITYI 181
Cdd:TIGR01043 82 YDGVQRPLDVLKEKTGD-FIARGVDAPGLDRDKKWHFKPTVK-EGDKVEGGDIIGVVPETSLIEHKILVPPNVEGEIVEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 182 APPGQYSLKDTVLELEFQGvKKKFTMLQTWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVI 261
Cdd:TIGR01043 160 AEEGDYTVEDTIAVVDTDG-DEEIKMYQKWPVRIPRPYKEKLPPEVPLITGQRILDTFFPIAKGGTAAIPGPFGSGKTVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 262 SQALSKYSNSDTVVYVGCGERGNEMAEVLMDFPQLtmtlPDGRE-ESVMKRTTLVANTSNMPVAAREASIYTGITIAEYF 340
Cdd:TIGR01043 239 QHQLAKWSDADIVVYIGCGERGNEMTDVLEEFPEL----KDPKTgKPLMERTVLIANTSNMPVAAREASIYTGITIAEYF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 341 RDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPERNGSVTIVGAVSPPGGDF 420
Cdd:TIGR01043 315 RDMGYDVALMADSTSRWAEAMREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEERVGSVTVIGAVSPPGGDF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 421 SDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTAL-ESFYEKFDSDFIDIRTKAREVLQREDDLNEIVQLV 499
Cdd:TIGR01043 395 SEPVTQNTLRIVKVFWALDADLAQRRHFPAINWLQSYSLYVDLVqDWWHENVDPDWREMRDEAMDLLQKESELQEIVQLV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 500 GKDALAETDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERGAGMDgqKITYTLIKHRLG 579
Cdd:TIGR01043 475 GPDALPERQKLILEVARMIREAFLQQNAFDPVDTYCPPQKQYRILRAIMNFYDEAMEALERGVPVE--EILKLEVKEEIG 552
|
570 580 590
....*....|....*....|....*....|....*..
gi 976921132 580 DLfyrlvsqKFEDPAEGEDvligKFKKLNEDLSAGFR 616
Cdd:TIGR01043 553 RM-------KYEPDNDILA----KIDEILEKIEKEFK 578
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
88-460 |
0e+00 |
|
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.
Pssm-ID: 410878 [Multi-domain] Cd Length: 288 Bit Score: 623.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 88 PLSVELGPGILGNIFDGIQRPLKTIAKrSGDVYIPRGVSVpaldkdilwefqpkkkgegdlitggdlyatvfenslvehh 167
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIAE-TGSIFIPRGVNV---------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 168 ialppdamgkityiappgqyslkdtvlelefqgvkkkftmlQTWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGT 247
Cdd:cd01134 40 -----------------------------------------QRWPVRQPRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGT 78
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 248 CAIPGAFGCGKTVISQALSKYSNSDTVVYVGCGERGNEMAEVLMDFPQLTMTLpdgREESVMKRTTLVANTSNMPVAARE 327
Cdd:cd01134 79 AAIPGPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMAEVLEEFPELKDPI---TGESLMERTVLIANTSNMPVAARE 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 328 ASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPERNGSV 407
Cdd:cd01134 156 ASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRCLGSPGREGSV 235
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 976921132 408 TIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKY 460
Cdd:cd01134 236 TIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSKY 288
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
259-611 |
3.66e-121 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 391.31 E-value: 3.66e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 259 TVISQALSKYSNSDTVVYVGCGERGNEMAEVLMDFPQLTmtlPDGREESVMKRTTLVANTSNMPVAAREASIYTGITIAE 338
Cdd:PRK14698 670 TVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPKLK---DPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 339 YFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPERNGSVTIVGAVSPPGG 418
Cdd:PRK14698 747 YFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSDYRVGSVSVIGAVSPPGG 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 419 DFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALESFYEK-FDSDFIDIRTKAREVLQREDDLNEIVQ 497
Cdd:PRK14698 827 DFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKnVDPEWKAMRDKAMELLQKEAELQEIVR 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 498 LVGKDALAETDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERGAGMdgQKITYTLIKHR 577
Cdd:PRK14698 907 IVGPDALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQVTMMRVLLNFYDKTMDAISRGVPL--EEIAKLPVREE 984
|
330 340 350
....*....|....*....|....*....|....
gi 976921132 578 LGDLfyrlvsqKFEDPAEGEDVLIGKFKKLNEDL 611
Cdd:PRK14698 985 IGRM-------KFEPDIEKIKALIDKTNEQFDEL 1011
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
232-458 |
1.19e-103 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 319.30 E-value: 1.19e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 232 GQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDTVVYVGCGERGNEMAEVLMDFPqltmtlpdgrEESVMKR 311
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELL----------GSGALKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 312 TTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYER 391
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976921132 392 AGKVKclggpERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYS 458
Cdd:pfam00006 151 AGRVK-----GKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
207-460 |
4.18e-90 |
|
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410884 [Multi-domain] Cd Length: 270 Bit Score: 285.89 E-value: 4.18e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 207 MLQTWPVRTPRP-VASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNS---DTVVYVGCGER 282
Cdd:cd19476 28 TKQRRPIHLKAPnPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQAKahaGVVVFAGIGER 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 283 GNEMAEVLMDFPqltmtlpdgrEESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALR 362
Cdd:cd19476 108 GREVNDLYEEFT----------KSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLIIDDISRYAEALR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 363 EISGRLAEMPADSGYPAYLAARLASFYERAGKVKclggpERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKL 442
Cdd:cd19476 178 EMSALLGEPPGREGYPPYLFTKLATLYERAGKVK-----DGGGSITAIPAVSTPGDDLTDPIPDNTFAILDGQIVLSREL 252
|
250
....*....|....*...
gi 976921132 443 AQRKHFPSVNWLISYSKY 460
Cdd:cd19476 253 ARKGIYPAINVLDSTSRV 270
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
22-260 |
2.21e-74 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 263.04 E-value: 2.21e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 22 GYVRKVSGPVVIADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILGNI 101
Cdd:PRK14698 5 GRIIRVTGPLVIADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPVEGTGSSLSVELGPGLLTSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 102 FDGIQRPLKTIAKRSGDvYIPRGVSVPALDKDILWEFQPKKKgEGDLITGGDLYATVFENSLVEHHIALPPDAMGKITYI 181
Cdd:PRK14698 85 YDGIQRPLEVIREKSGD-FIARGISAPALPRDKKWHFIPKVK-VGDKVVGGDIIGEVPETSIITHKIMVPPGIEGEIVEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 182 APPGQYSLKDTVLELEF-QGVKKKFTMLQTWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTV 260
Cdd:PRK14698 163 ADEGEYTIEEVIAKVKTpSGEIKELKMYQRWPVRVKRPYKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKCV 242
|
|
| ATP-synt_ab_Xtn |
pfam16886 |
ATPsynthase alpha/beta subunit N-term extension; ATP-synt_ab_Xtn is an extension of the ... |
102-223 |
1.68e-63 |
|
ATPsynthase alpha/beta subunit N-term extension; ATP-synt_ab_Xtn is an extension of the alpha-beta catalytic subunit of VATA or V-type proton ATPase catalytic subunit at the N-terminal end. It is found from bacteria to humans, and was not modelled in family ATP-synt_ab, pfam00006.
Pssm-ID: 465299 [Multi-domain] Cd Length: 120 Bit Score: 208.79 E-value: 1.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 102 FDGIQRPLKTIAKRSGDvYIPRGVSVPALDKDILWEFQPKKKgEGDLITGGDLYATVFENSLVEHHIALPPDAMGKITYI 181
Cdd:pfam16886 1 FDGIQRPLEKIAEKSGS-FIPRGVDVPALDREKKWEFTPTVK-VGDKVSGGDILGTVQETSLIEHKIMVPPGVSGTVTEI 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 976921132 182 APPGQYSLKDTVLELEFQGVKKKFTMLQTWPVRTPRPVASKL 223
Cdd:pfam16886 79 APEGEYTVEDTIAEVEDEGKEKELTMMQKWPVRRPRPYKEKL 120
|
|
| ATP-synt_V_A-type_alpha_C |
cd18111 |
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of ... |
475-581 |
3.59e-51 |
|
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of the V1/A1 complex of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes.
Pssm-ID: 349746 [Multi-domain] Cd Length: 105 Bit Score: 174.11 E-value: 3.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 475 FIDIRTKAREVLQREDDLNEIVQLVGKDALAETDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLA 554
Cdd:cd18111 1 WVELRTEAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIREDFLQQNAFDEVDTYCPLEKQYKMLKLILTFYDKA 80
|
90 100
....*....|....*....|....*..
gi 976921132 555 NQAVERGAGMDgqKITYTLIKHRLGDL 581
Cdd:cd18111 81 LEALEKGVPLS--KILELPVREKIARM 105
|
|
| fliI_yscN |
TIGR01026 |
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ... |
8-532 |
2.77e-42 |
|
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP synthase F1, beta subunit. It is a mixture of members with two different protein functions. The first group is exemplified by Salmonella typhimurium FliI protein. It is needed for flagellar assembly, its ATPase activity is required for flagellation, and it may be involved in a specialized protein export pathway that proceeds without signal peptide cleavage. The second group of proteins function in the export of virulence proteins; exemplified by Yersinia sp. YscN protein an ATPase involved in the type III secretory pathway for the antihost Yops proteins. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 273401 [Multi-domain] Cd Length: 440 Bit Score: 160.23 E-value: 2.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 8 RLTTFEDSEKESECGYVRKVSGPVVIADGMAgAAMYELVRV----GHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVL 83
Cdd:TIGR01026 11 RLCQEMDLRLVKRVGRVTKVKGLLIEAVGPQ-ASVGDLCLIerrgSEGRLVAEVVGFNGEFVFLMPYEEVEGVRPGSKVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 84 RTHKPLSVELGPGILGNIFDGIQRPLKTiakrsgdvyiprgvsvpaldkdilwefqpkkkgegdlitGGDLYATVFENSL 163
Cdd:TIGR01026 90 ATGEGLSIKVGDGLLGRVLDGLGKPIDG---------------------------------------KGKFLDNVETEGL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 164 vehhIALPPDAMGkityiappgqyslkdtvlelefqgvkkkftmlqtwpvRTPrpvasklaADTPLLTGQRVLDALFPSV 243
Cdd:TIGR01026 131 ----ITAPINPLK-------------------------------------RAP--------IREILSTGVRSIDGLLTVG 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 244 LGGTCAIPGAFGCGKTVISQALSKYSNSDTVVYVGCGERGNEmaevLMDFPQltmtlPDGREESvMKRTTLVANTSNMPV 323
Cdd:TIGR01026 162 KGQRIGIFAGSGVGKSTLLGMIARNTEADVNVIALIGERGRE----VREFIE-----HDLGEEG-LKRSVVVVATSDQSP 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 324 AAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKvkclggpER 403
Cdd:TIGR01026 232 LLRLKGAYVATAIAEYFRDQGKDVLLLMDSVTRFAMAQREIGLAAGEPPATKGYTPSVFSTLPRLLERAGA-------SG 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 404 NGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALESfyekfdSDFIDIRTKAR 483
Cdd:TIGR01026 305 KGSITAFYTVLVEGDDMNEPIADSVRGILDGHIVLSRALAQRGHYPAIDVLASISRLMTAIVS------EEHRRAARKFR 378
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 976921132 484 EVL---QREDDLNEI-VQLVGKDalAETDKITLETAKLlrEDYLAQNAFTPYD 532
Cdd:TIGR01026 379 ELLskyKDNEDLIRIgAYQRGSD--RELDFAIAKYPKL--ERFLKQGINEKVN 427
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
29-533 |
3.19e-40 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 154.20 E-value: 3.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 29 GPVVIADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILGNIFDGIQRP 108
Cdd:PRK06820 37 GPTLLRASLPGVAQGELCRIEPQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 109 LktiakrsgDVYIPRGVSVPALDkdilwefqpkkkgegdlitggdlyatvfenslvehhialppdamgkityiAPPgqys 188
Cdd:PRK06820 117 I--------DGGPPLTGQWRELD--------------------------------------------------CPP---- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 189 lkdtvlelefqgvkkkftmlqtwpvrtPRPVASKLAaDTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKY 268
Cdd:PRK06820 135 ---------------------------PSPLTRQPI-EQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCAD 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 269 SNSDTVVYVGCGERGNEMAEvlmdFPQLTMTlPDGREesvmkRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVS 348
Cdd:PRK06820 187 SAADVMVLALIGERGREVRE----FLEQVLT-PEARA-----RTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVL 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 349 MMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAgkvkclgGPERNGSVTIVGAVSPPGGDFSDPVTSAT 428
Cdd:PRK06820 257 LMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERT-------GNSDRGSITAFYTVLVEGDDMNEPVADEV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 429 LSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALESFYEKFDSdfidirTKAREVLQREDDLNEIVQlVG---KDALA 505
Cdd:PRK06820 330 RSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMA------QKLRRMLACYQEIELLVR-VGeyqAGEDL 402
|
490 500 510
....*....|....*....|....*....|
gi 976921132 506 ETDKiTLETAKLLReDYLAQ--NAFTPYDK 533
Cdd:PRK06820 403 QADE-ALQRYPAIC-AFLQQdhSETAHLET 430
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
21-452 |
3.33e-40 |
|
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440771 [Multi-domain] Cd Length: 433 Bit Score: 154.03 E-value: 3.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 21 CGYVRKVSGPVVIADGMaGAAMYELVRV---GHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGI 97
Cdd:COG1157 20 SGRVTRVVGLLIEAVGP-DASIGELCEIetaDGRPVLAEVVGFRGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGDGL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 98 LGNIFDGIQRPLktiakrsgdvyiprgvsvpaldkDilwefqpkkkGEGDLiTGGDLYATvfenslvehhIALPPDAMGK 177
Cdd:COG1157 99 LGRVLDGLGRPL-----------------------D----------GKGPL-PGEERRPL----------DAPPPNPLER 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 178 ityiappgqyslkdtvlelefqgvkkkftmlqtwpvrtpRPVasklaaDTPLLTGQRVLDALFPSVLG---GTCAipGAf 254
Cdd:COG1157 135 ---------------------------------------ARI------TEPLDTGVRAIDGLLTVGRGqriGIFA--GS- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 255 GCGKTVISQALSKYSNSDTVVyVG-CGERGNEmaevLMDFpqLTMTL-PDGreesvMKRTTLVANTSNMPVAAREASIYT 332
Cdd:COG1157 167 GVGKSTLLGMIARNTEADVNV-IAlIGERGRE----VREF--IEDDLgEEG-----LARSVVVVATSDEPPLMRLRAAYT 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 333 GITIAEYFRDMGYNVSMMADSTSRWAEALREISgrLA--EMPADSGYPAYLAARLASFYERAgkvkclgGPERNGSVTIV 410
Cdd:COG1157 235 ATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIG--LAagEPPATRGYPPSVFALLPRLLERA-------GNGGKGSITAF 305
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 976921132 411 GAVSPPGGDFSDPVTSATLSI-----VqvfwgLDKKLAQRKHFPSVN 452
Cdd:COG1157 306 YTVLVEGDDMNDPIADAVRGIldghiV-----LSRKLAERGHYPAID 347
|
|
| ATP-synt_V_A-type_alpha_N |
cd18119 |
V/A-type ATP synthase catalytic subunit A (alpha), N-terminal domain; The alpha (A) subunit of ... |
22-87 |
5.54e-40 |
|
V/A-type ATP synthase catalytic subunit A (alpha), N-terminal domain; The alpha (A) subunit of the V1/A1 complexes of V/A-type ATP synthases, N-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 or A1 complex contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes.
Pssm-ID: 349743 [Multi-domain] Cd Length: 67 Bit Score: 141.51 E-value: 5.54e-40
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 976921132 22 GYVRKVSGPVVIADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHK 87
Cdd:cd18119 2 GKIYRVSGPVVVAEGMSGAAMYELVRVGEEGLIGEIIRLEGDKATIQVYEETSGLKVGEPVERTGK 67
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
209-459 |
9.44e-40 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 148.09 E-value: 9.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 209 QTWPVRTPRPVASKLAA-DTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDTVVYVGCGERGNEma 287
Cdd:cd01136 30 ERRPLIAAPPNPLKRAPiEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIARNTDADVNVIALIGERGRE-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 288 evLMDFPQLTMtlpdgrEESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGR 367
Cdd:cd01136 108 --VREFIEKDL------GEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLMDSLTRFAMAQREVGLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 368 LAEMPADSGYPAYLAARLASFYERAgkvkclgGPERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKH 447
Cdd:cd01136 180 AGEPPTRRGYPPSVFALLPRLLERA-------GNGEKGSITAFYTVLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGH 252
|
250
....*....|..
gi 976921132 448 FPSVNWLISYSK 459
Cdd:cd01136 253 YPAIDVLASISR 264
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
210-528 |
1.51e-37 |
|
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 211621 [Multi-domain] Cd Length: 461 Bit Score: 147.17 E-value: 1.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 210 TWPVRTPRPVASKLAADTPLL-TGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSK---YSNSDTVVYVGCGER--- 282
Cdd:TIGR01039 107 RWPIHRKAPSFEEQSTKVEILeTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINniaKEHGGYSVFAGVGERtre 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 283 GN----EMAEvlmdfpqltmtlpdgreESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDM-GYNVSMMADSTSRW 357
Cdd:TIGR01039 187 GNdlyhEMKE-----------------SGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEqGQDVLLFIDNIFRF 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 358 AEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKclggperNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWG 437
Cdd:TIGR01039 250 TQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTK-------TGSITSVQAVYVPADDLTDPAPATTFAHLDATTV 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 438 LDKKLAQRKHFPSVNWLISYSKYSTAL---ESFYekfdsdfiDIRTKAREVLQREDDLNEIVQLVGKDALAETDKITLET 514
Cdd:TIGR01039 323 LSRKIAELGIYPAVDPLDSTSRLLDPSvvgEEHY--------DVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVER 394
|
330
....*....|....
gi 976921132 515 AKLLrEDYLAQNAF 528
Cdd:TIGR01039 395 ARRI-QRFLSQPFF 407
|
|
| FliI_clade1 |
TIGR03496 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
22-458 |
3.27e-34 |
|
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of bacterial flagellum systems. This protein acts to drive protein export for flagellar biosynthesis. The most closely related family is the YscN family of bacterial type III secretion systems. This model represents one (of three) segment of the FliI family tree. These have been modeled separately in order to exclude the type III secretion ATPases more effectively. [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274607 [Multi-domain] Cd Length: 411 Bit Score: 136.07 E-value: 3.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 22 GYVRKVSGPVVIADGMAGA--AMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILG 99
Cdd:TIGR03496 1 GRVTRVVGLVLEAVGLRAPvgSRCEIESSDGDPIEAEVVGFRGDRVLLMPLEDVEGLRPGARVFPLGGPLRLPVGDSLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 100 NIFDGIQRPLktiakrSGDVYIPRGVSVPAldkdilwefqpkkkgegdlitggdlyatvfenslvehhIALPPDAMGKit 179
Cdd:TIGR03496 81 RVIDGLGRPL------DGKGPLDAGERVPL--------------------------------------YAPPINPLKR-- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 180 yiappgqyslkdtvlelefqgvkkkftmlqtwpvrtpRPVasklaaDTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKT 259
Cdd:TIGR03496 115 -------------------------------------API------DEPLDVGVRAINGLLTVGRGQRMGIFAGSGVGKS 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 260 VISQALSKYSNSDTVVyVG-CGERGNEMAEVLMDfpqltmTLPdgreESVMKRTTLVANTSNMPVAAREASIYTGITIAE 338
Cdd:TIGR03496 152 TLLGMMARYTEADVVV-VGlIGERGREVKEFIED------ILG----EEGLARSVVVAATADESPLMRLRAAFYATAIAE 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 339 YFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKvkclgGPERNGSVTIVGAVSPPGG 418
Cdd:TIGR03496 221 YFRDQGKDVLLLMDSLTRFAMAQREIALAIGEPPATKGYPPSVFAKLPQLVERAGN-----GEEGKGSITAFYTVLVEGD 295
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 976921132 419 DFSDPVTSATLSIVQvfwG---LDKKLAQRKHFPSVNWLISYS 458
Cdd:TIGR03496 296 DQQDPIADAARAILD---GhivLSRELAEQGHYPAIDILASIS 335
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
216-498 |
2.84e-32 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 130.50 E-value: 2.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 216 PRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDTVVYVGCGERGNEMAEvlmdFPQ 295
Cdd:PRK08149 122 PPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEHSEADVFVIGLIGERGREVTE----FVE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 296 lTMTLPDGREesvmkRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADS 375
Cdd:PRK08149 198 -SLRASSRRE-----KCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARR 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 376 GYPAYLAARLASFYERAGKVKclggperNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLI 455
Cdd:PRK08149 272 GYPASVFDSLPRLLERPGATL-------AGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLK 344
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 976921132 456 SYSKYstalesFYEKFDSDFIDIRTKAREVLQREDDLNEIVQL 498
Cdd:PRK08149 345 SVSRV------FGQVTDPKHRQLAAAFRKLLTRLEELQLFIDL 381
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
37-459 |
5.80e-32 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 129.69 E-value: 5.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 37 MAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILGNIFDGIQRPLKtiakrs 116
Cdd:PRK07594 37 LPGVFMGELCCIKPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLD------ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 117 gdvyiprGVSVPaldkDILWEfqpkkkgEGDlitggdlyatvfenslvehhiALPPDAMgkityiappgqyslkdtvlel 196
Cdd:PRK07594 111 -------GRELP----DVCWK-------DYD---------------------AMPPPAM--------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 197 efqgvkkkftmlqtwpvrTPRPVASklaadtPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDTVVY 276
Cdd:PRK07594 131 ------------------VRQPITQ------PLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDADSNVL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 277 VGCGERGNEMAEvlmdFPQLTMTlpdgreESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSR 356
Cdd:PRK07594 187 VLIGERGREVRE----FIDFTLS------EETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTR 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 357 WAEALREISGRLAEMPADSGYPAYLAARLASFYERAGkvkcLGgpeRNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFW 436
Cdd:PRK07594 257 YARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG----MG---EKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHI 329
|
410 420
....*....|....*....|...
gi 976921132 437 GLDKKLAQRKHFPSVNWLISYSK 459
Cdd:PRK07594 330 VLSRRLAERGHYPAIDVLATLSR 352
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
216-506 |
1.50e-31 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 128.72 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 216 PRPVASKLAaDTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDTVVYVGCGERGNEMAEVLMDfpq 295
Cdd:PRK06936 134 PAPMSRRLI-ETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRSAEVDVTVLALIGERGREVREFIES--- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 296 ltmtlpDGREESvMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADS 375
Cdd:PRK06936 210 ------DLGEEG-LRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRR 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 376 GYPAYLAARLASFYERAgkvkclgGPERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLI 455
Cdd:PRK06936 283 GYPPSVFAALPRLMERA-------GQSDKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLR 355
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 976921132 456 SYSKYSTALESFYEKFDSDfidirtKAREVLQREDDLNEIVQL----VGKDALAE 506
Cdd:PRK06936 356 SASRVMNQIVSKEHKTWAG------RLRELLAKYEEVELLLQIgeyqKGQDKEAD 404
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
215-459 |
8.45e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 126.65 E-value: 8.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 215 TPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDTVVYVGCGERGNEMAEVLMDfp 294
Cdd:PRK06002 135 TAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDTVVIALVGERGREVREFLED-- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 295 qltmTLPDGREESVmkrtTLVANTSNMPVAAREASIyTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPAD 374
Cdd:PRK06002 213 ----TLADNLKKAV----AVVATSDESPMMRRLAPL-TATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVA 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 375 SGYPAYLAARLASFYERAGKvkclgGPERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWL 454
Cdd:PRK06002 284 RGYPPSVFSELPRLLERAGP-----GAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPL 358
|
....*
gi 976921132 455 ISYSK 459
Cdd:PRK06002 359 ASISR 363
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
212-498 |
9.35e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 126.25 E-value: 9.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 212 PVRTPRPVA-SKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDTVVYVGCGERGNEMAEVL 290
Cdd:PRK08927 124 PLRAPPPPAhSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADADVSVIGLIGERGREVQEFL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 291 MDfpqltmTL-PDGreesvMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLA 369
Cdd:PRK08927 204 QD------DLgPEG-----LARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAG 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 370 EMPADSGYPAYLAARLASFYERAGKvkclgGPERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFP 449
Cdd:PRK08927 273 EPPTTKGYTPTVFAELPRLLERAGP-----GPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYP 347
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 976921132 450 SVNWLISYSKysTALESfyekFDSDFIDIRTKAREVLQREDDLNEIVQL 498
Cdd:PRK08927 348 AINVLKSVSR--TMPGC----NDPEENPLVRRARQLMATYADMEELIRL 390
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
227-459 |
8.09e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 120.60 E-value: 8.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 227 TPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDTVVYVGCGERGNEMAEVL-MDFPqltmtlPDGre 305
Cdd:PRK07721 140 EPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIARNTSADLNVIALIGERGREVREFIeRDLG------PEG-- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 306 esvMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARL 385
Cdd:PRK07721 212 ---LKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAIL 288
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 976921132 386 ASFYERAGKvkclggpERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSK 459
Cdd:PRK07721 289 PKLLERTGT-------NASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSR 355
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
21-548 |
3.44e-28 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 118.72 E-value: 3.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 21 CGYVRKVSGPVVIADGMAgAAMYEL--VRVGHDNLI--GEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPG 96
Cdd:PRK09099 25 TGKVVEVIGTLLRVSGLD-VTLGELceLRQRDGTLLqrAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLSVPVGPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 97 ILGNIFDGIQRPLKtiakrsgdvyiprgvSVPALDKDilwEFQPKkkgegdlitggdlyatvfenslvehhIALPPDAMg 176
Cdd:PRK09099 104 LLGRVIDGLGEPID---------------GGGPLDCD---ELVPV--------------------------IAAPPDPM- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 177 kityiappgqyslkdtvlelefqgvkkkftmlqtwpvrtprpvaSKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGC 256
Cdd:PRK09099 139 --------------------------------------------SRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGV 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 257 GKTVISQALSKYSNSDTVVYVGCGERGNEMAEvlmdFPQLTMTlPDGreesvMKRTTLVANTSNMPVAAREASIYTGITI 336
Cdd:PRK09099 175 GKSTLMGMFARGTQCDVNVIALIGERGREVRE----FIELILG-EDG-----MARSVVVCATSDRSSIERAKAAYVATAI 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 337 AEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKvkclggpERNGSVTIVGAVSPP 416
Cdd:PRK09099 245 AEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM-------GETGSITALYTVLAE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 417 GGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALesfyekFDSDFIDIRTKAREVLQREDDLNEIV 496
Cdd:PRK09099 318 DESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQV------VPREHVQAAGRLRQLLAKHREVETLL 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 976921132 497 QL----VGKDALAETdkiTLETAKLLReDYLAQnaftPYDKFCPFYKSVWMMRNII 548
Cdd:PRK09099 392 QVgeyrAGSDPVADE---AIAKIDAIR-DFLSQ----RTDEYSDPDATLAALAELS 439
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
24-525 |
4.38e-28 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 118.78 E-value: 4.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 24 VRKVSGPVVIADGMAGAAMYELVRVGHDN---LIGEIIRLEGDSATIQVYEETAGLMVNDPVLR-THKPLSVELGPGILG 99
Cdd:PRK04196 7 VSEIKGPLLFVEGVEGVAYGEIVEIELPNgekRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRfTGEPLKLPVSEDMLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 100 NIFDGIQRPL----KTIAKRSGDV---------------YIPRGVSvpALDkdilwefqpkkkGEGDLITGGDLyaTVFE 160
Cdd:PRK04196 87 RIFDGLGRPIdggpEIIPEKRLDIngapinpvareypeeFIQTGIS--AID------------GLNTLVRGQKL--PIFS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 161 NSlvehhiALPpdamgkityiappgqyslkdtvlelefqgvkkkftmlqtwpvrtprpvASKLAAdtplltgQRVLDAlf 240
Cdd:PRK04196 151 GS------GLP------------------------------------------------HNELAA-------QIARQA-- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 241 pSVLGGTcaipgafgcgktvisqalSKYSnsdtVVYVGCGERgNEMAEVLMDfpqltmtlpDGREESVMKRTTLVANTSN 320
Cdd:PRK04196 168 -KVLGEE------------------ENFA----VVFAAMGIT-FEEANFFME---------DFEETGALERSVVFLNLAD 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 321 MPVAAREASIYTGITIAEYFR-DMGYNV-SMMADSTSrWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKcl 398
Cdd:PRK04196 215 DPAIERILTPRMALTAAEYLAfEKGMHVlVILTDMTN-YCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIK-- 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 399 ggpERNGSVTIVGAVSPPGGDFSDPVTSATLSIV--QVFwgLDKKLAQRKHFPSVNWLISYSkystalesfyeKFDSDFI 476
Cdd:PRK04196 292 ---GKKGSITQIPILTMPDDDITHPIPDLTGYITegQIV--LSRELHRKGIYPPIDVLPSLS-----------RLMKDGI 355
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 976921132 477 DirtkarEVLQRED----------------DLNEIVQLVGKDALAETDKITLETAKLLREDYLAQ 525
Cdd:PRK04196 356 G------EGKTREDhkdvanqlyaayargkDLRELAAIVGEEALSERDRKYLKFADAFEREFVNQ 414
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
24-525 |
6.13e-28 |
|
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 440770 [Multi-domain] Cd Length: 462 Bit Score: 118.32 E-value: 6.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 24 VRKVSGPVVIADGMAGAAMYELVRV-GHDNLI--GEIIRLEGDSATIQVYEETAGLMVNDPVLR-THKPLSVELGPGILG 99
Cdd:COG1156 9 ISEIAGPLLFVEGVEGVGYGELVEIeLPDGERrrGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRfLGEPLELPVSEDMLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 100 NIFDGIQRPL----KTIAKRSGDV---------------YIPRGVSvpALDkdilwefqpkkkGEGDLITGGDLyaTVFE 160
Cdd:COG1156 89 RVFNGLGRPIdggpPIIPEKRLDIngspinpvareypreFIQTGIS--AID------------GLNTLVRGQKL--PIFS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 161 NSlvehhiALPpdamgkityiappgqyslkdtvlelefqgvkkkftmlqtwpvrtprpvASKLAAdtplltgQRVLDAlf 240
Cdd:COG1156 153 GS------GLP------------------------------------------------HNELAA-------QIARQA-- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 241 pSVLGGTcaipGAFGcgktvisqalskysnsdtVVYVGCGERGNEMAEVLMDFpqltmtlpdgrEES-VMKRTTLVANTS 319
Cdd:COG1156 170 -KVRGEE----EKFA------------------VVFAAMGITHDEANFFREEF-----------EETgALDRVVMFLNLA 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 320 NMPVAAREASIYTGITIAEYFR-DMGYNV-SMMADSTSrWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKc 397
Cdd:COG1156 216 DDPAIERIITPRMALTAAEYLAfEKGMHVlVILTDMTN-YCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIK- 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 398 lggpERNGSVTIVGAVSPPGGDFSDPVTSATLSIV--QVFwgLDKKLAQRKHFPSVNWLISYSkystalesfyekfdsdf 475
Cdd:COG1156 294 ----GRKGSITQIPILTMPNDDITHPIPDLTGYITegQIV--LSRDLHRKGIYPPIDVLPSLS----------------- 350
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 976921132 476 idiRTKAR---EVLQRED----------------DLNEIVQLVGKDALAETDKITLETAKLLREDYLAQ 525
Cdd:COG1156 351 ---RLMKDgigEGKTREDhadvanqlyaayargqEVRELAAIVGEEALSETDKKYLKFADAFERRFVNQ 416
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
255-452 |
9.04e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 114.41 E-value: 9.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 255 GCGKTVISQALSKYSNSDTVVyVG-CGERGNEMAEVLMDFpqLTmtlPDGREESVmkrttLVANTSNMPVAAREASIYTG 333
Cdd:PRK08972 172 GVGKSVLLGMMTRGTTADVIV-VGlVGERGREVKEFIEEI--LG---EEGRARSV-----VVAAPADTSPLMRLKGCETA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 334 ITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKvkclgGPERNGSVTIVGAV 413
Cdd:PRK08972 241 TTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGN-----GGPGQGSITAFYTV 315
|
170 180 190
....*....|....*....|....*....|....*....
gi 976921132 414 SPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVN 452
Cdd:PRK08972 316 LTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAID 354
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
209-529 |
1.89e-26 |
|
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439825 [Multi-domain] Cd Length: 468 Bit Score: 113.65 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 209 QTWPVRTPRPVASKLAADTPLL-TGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQAL--------SKYSnsdtvVYVGC 279
Cdd:COG0055 109 ERRPIHRPAPPFEEQSTKTEILeTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELihniakehGGVS-----VFAGV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 280 GER---GNEMaevlmdfpQLTMtlpdgREESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRD-MGYNVSMMADSTS 355
Cdd:COG0055 184 GERtreGNDL--------YREM-----KESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFIDNIF 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 356 RWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKclggperNGSVTIVGAVSPPGGDFSDPVTSATLS----- 430
Cdd:COG0055 251 RFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTK-------KGSITSVQAVYVPADDLTDPAPATTFAhldat 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 431 IVqvfwgLDKKLAQRKHFPSVNWLISYSKYSTAL---ESFYekfdsdfiDIRTKAREVLQREDDLNEIVQLVGKDALAET 507
Cdd:COG0055 324 TV-----LSRKIAELGIYPAVDPLDSTSRILDPLivgEEHY--------RVAREVQRILQRYKELQDIIAILGMDELSEE 390
|
330 340
....*....|....*....|...
gi 976921132 508 DKITLETA-KLLRedYLAQNAFT 529
Cdd:COG0055 391 DKLTVARArKIQR--FLSQPFFV 411
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
209-459 |
6.26e-26 |
|
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410877 [Multi-domain] Cd Length: 277 Bit Score: 108.46 E-value: 6.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 209 QTWPVRTPRPVASKLAADTPLL-TGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQAL----SKySNSDTVVYVGCGERG 283
Cdd:cd01133 30 ERWPIHREAPEFVELSTEQEILeTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinniAK-AHGGYSVFAGVGERT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 284 NEMAEVLMDfpqltMTLPDGREESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDM-GYNVSMMADSTSRWAEALR 362
Cdd:cd01133 109 REGNDLYHE-----MKESGVINLDGLSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEeGQDVLLFIDNIFRFTQAGS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 363 EISGRLAEMPADSGYPAYLAARLASFYERAGKVKclggperNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKL 442
Cdd:cd01133 184 EVSALLGRIPSAVGYQPTLATEMGSLQERITSTK-------KGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGI 256
|
250
....*....|....*..
gi 976921132 443 AQRKHFPSVNWLISYSK 459
Cdd:cd01133 257 AELGIYPAVDPLDSTSR 273
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
226-459 |
3.36e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 103.66 E-value: 3.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 226 DTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDTVVYVGCGERGNEMAEVLMDFpqltmtlpdgRE 305
Cdd:PRK05688 149 SEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEADIIVVGLIGERGREVKEFIEHI----------LG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 306 ESVMKRTTLVANTSN-MPVAAREASIYTgITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAAR 384
Cdd:PRK05688 219 EEGLKRSVVVASPADdAPLMRLRAAMYC-TRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAK 297
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 976921132 385 LASFYERAGKvkclgGPERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSK 459
Cdd:PRK05688 298 LPKLVERAGN-----AEPGGGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISR 367
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
209-528 |
9.22e-23 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 102.81 E-value: 9.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 209 QTWPVRTPRPVASKLaaDTPLL---TGQRVLDALFPSVLGGTCAIPGAFGCGKTV--------ISQALSKYSnsdtvVYV 277
Cdd:CHL00060 124 TTSPIHRSAPAFIQL--DTKLSifeTGIKVVDLLAPYRRGGKIGLFGGAGVGKTVlimelinnIAKAHGGVS-----VFG 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 278 GCGERGNEMAEVLMDFPQLTMTLPDGREESvmkRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGY-NVSMMADSTSR 356
Cdd:CHL00060 197 GVGERTREGNDLYMEMKESGVINEQNIAES---KVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFR 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 357 WAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKclggperNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFW 436
Cdd:CHL00060 274 FVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTK-------EGSITSIQAVYVPADDLTDPAPATTFAHLDATT 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 437 GLDKKLAQRKHFPSVNWLISyskYSTAL------ESFYEkfdsdfidIRTKAREVLQREDDLNEIVQLVGKDALAETDKI 510
Cdd:CHL00060 347 VLSRGLAAKGIYPAVDPLDS---TSTMLqprivgEEHYE--------TAQRVKQTLQRYKELQDIIAILGLDELSEEDRL 415
|
330
....*....|....*...
gi 976921132 511 TLETAKLLrEDYLAQNAF 528
Cdd:CHL00060 416 TVARARKI-ERFLSQPFF 432
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
263-459 |
5.73e-22 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 96.91 E-value: 5.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 263 QA-LSKYSNSDTVVYVGCGERgNEMAEVLMDfpqltmtlpDGREESVMKRTTLVANTSNMPVAAReasIYT---GITIAE 338
Cdd:cd01135 92 QAgVVGSEENFAIVFAAMGVT-MEEARFFKD---------DFEETGALERVVLFLNLANDPTIER---IITprmALTTAE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 339 YFR-DMGYNV-SMMADSTSrWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKclggpERNGSVTIVGAVSPP 416
Cdd:cd01135 159 YLAyEKGKHVlVILTDMTN-YAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVE-----GRKGSITQIPILTMP 232
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 976921132 417 GGDFSDPVTSATLSIV--QVFwgLDKKLAQRKHFPSVNWLISYSK 459
Cdd:cd01135 233 NDDITHPIPDLTGYITegQIY--LDRDLHNKGIYPPIDVLPSLSR 275
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
229-464 |
7.01e-22 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 99.86 E-value: 7.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 229 LLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDTVVYVGCGERGNEMAevlmDFPQLTMTlPDGREESV 308
Cdd:PRK07960 159 LDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVK----DFIENILG-AEGRARSV 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 309 MkrttLVANTSNMPVAAREASIYtGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASF 388
Cdd:PRK07960 234 V----IAAPADVSPLLRMQGAAY-ATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPAL 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 976921132 389 YERAGKvkclgGPERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTAL 464
Cdd:PRK07960 309 VERAGN-----GISGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAL 379
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
222-459 |
8.95e-22 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 99.19 E-value: 8.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 222 KLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDTVVYVGCGERGNEMAEVLMDFPQltmtlp 301
Cdd:PRK07196 132 RRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYTQADVVVVGLIGERGREVKEFIEHSLQ------ 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 302 dgrEESVMKRTTLVANTSNMPVAAREASIYTGiTIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYL 381
Cdd:PRK07196 206 ---AAGMAKSVVVAAPADESPLMRIKATELCH-AIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSA 281
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 976921132 382 AARLASFYERAGKvkclggPERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSK 459
Cdd:PRK07196 282 FSIIPRLAESAGN------SSGNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISR 353
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
208-459 |
4.92e-19 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 90.81 E-value: 4.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 208 LQTWPVRTPRPVASKLAADTPLL-TGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDTVVYVGCGERGNEM 286
Cdd:PRK06793 118 LQKIKLDAPPIHAFEREEITDVFeTGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGERGREV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 287 AevlmDFPQLTMTlpdgreESVMKRTTLVANTSNMP--VAAREASIYTgiTIAEYFRDMGYNVSMMADSTSRWAEALREI 364
Cdd:PRK06793 198 K----DFIRKELG------EEGMRKSVVVVATSDEShlMQLRAAKLAT--SIAEYFRDQGNNVLLMMDSVTRFADARRSV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 365 SGRLAEMPAdSGYPAYLAARLASFYERAGKVKclggperNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQ 444
Cdd:PRK06793 266 DIAVKELPI-GGKTLLMESYMKKLLERSGKTQ-------KGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELAT 337
|
250
....*....|....*
gi 976921132 445 RKHFPSVNWLISYSK 459
Cdd:PRK06793 338 LSHYPAISVLDSVSR 352
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
226-459 |
9.52e-19 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 89.74 E-value: 9.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 226 DTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDTVVYVGCGERGNEMAEvlmdFPQLTMtlpDGRE 305
Cdd:PRK08472 138 DEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGCLAPIKVVALIGERGREIPE----FIEKNL---GGDL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 306 ESvmkrTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARL 385
Cdd:PRK08472 211 EN----TVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLL 286
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 976921132 386 ASFYERAGKvkclggPERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSK 459
Cdd:PRK08472 287 PQLMERAGK------EEGKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASR 354
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
7-408 |
1.84e-18 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 89.59 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 7 ARLTTFEDSEKESECGYVRKVSGPVVIADGMAGAAMYELVRVGhDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTH 86
Cdd:PRK13343 14 QRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFE-GGSRGFAFNLEEELVGAVLLDDTADILAGTEVRRTG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 87 KPLSVELGPGILGNIFDGIQRPLKtiakrsgdvyiprgvsvpaldkdilwefqpkkkGEGdlitggdlyatvfenslveh 166
Cdd:PRK13343 93 RVLEVPVGDGLLGRVIDPLGRPLD---------------------------------GGG-------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 167 hiALPPDAMGKITYIAPPgqyslkdtVLELEFqgvkkkftmlqtwpvrtprpvasklaADTPLLTGQRVLDALFPSVLGG 246
Cdd:PRK13343 120 --PLQATARRPLERPAPA--------IIERDF--------------------------VTEPLQTGIKVVDALIPIGRGQ 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 247 TCAIPGAFGCGKT------VISQalskySNSDTV-VYVGCGERGNEMAEVLMdfpqltmTLpdgREESVMKRTTLVANTS 319
Cdd:PRK13343 164 RELIIGDRQTGKTaiaidaIINQ-----KDSDVIcVYVAIGQKASAVARVIE-------TL---REHGALEYTTVVVAEA 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 320 NMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPA---YLAARLasfYERAGKV- 395
Cdd:PRK13343 229 SDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGdifYLHSRL---LERAAKLs 305
|
410
....*....|...
gi 976921132 396 KCLGGpernGSVT 408
Cdd:PRK13343 306 PELGG----GSLT 314
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
302-528 |
2.02e-18 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 89.01 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 302 DGREESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFR-DMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAY 380
Cdd:TIGR01040 203 DFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGY 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 381 LAARLASFYERAGKVKclggpERNGSVTIVGAVSPPGGDFSDPVTSATLSIV--QVFwgLDKKLAQRKHFPSVNWLISYS 458
Cdd:TIGR01040 283 MYTDLATIYERAGRVE-----GRNGSITQIPILTMPNDDITHPIPDLTGYITegQIY--VDRQLHNRQIYPPINVLPSLS 355
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 976921132 459 KY--STALESFYEKfdsDFIDIRTKAREVLQREDDLNEIVQLVGKDALAETDKITLETAKLLREDYLAQNAF 528
Cdd:TIGR01040 356 RLmkSAIGEGMTRK---DHSDVSNQLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKNFIAQGPY 424
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
20-464 |
7.01e-17 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 84.19 E-value: 7.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 20 ECGYVRKVSGPVVIADGMAgAAMYELVRVG---HDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPG 96
Cdd:PRK05922 19 ECGLLSRVSGNLLEAQGLS-ACLGELCQISlskSPPILAEVIGFHNRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSDH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 97 ILGNIFDGIQRPLktiakrSGDVYIPRGVSVPAldkdilwefqpkkkgegdlitggdlyatvfenslvehhIALPPDAMG 176
Cdd:PRK05922 98 LLGRVLDGFGNPL------DGKEQLPKTHLKPL--------------------------------------FSSPPSPMS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 177 kityiappgqyslkdtvlelefqgvkkkftmlqtwpvRTPrpvasklaADTPLLTGQRVLDALFPSVLGGTCAIPGAFGC 256
Cdd:PRK05922 134 -------------------------------------RQP--------IQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGS 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 257 GKTVISQALSKYSNSDTVVYVGCGERGNEMAEVLMDFpqltmtlpdgREESVMKRTTLVANTSNMPVAAREASIYTGITI 336
Cdd:PRK05922 169 GKSSLLSTIAKGSKSTINVIALIGERGREVREYIEQH----------KEGLAAQRTIIIASPAHETAPTKVIAGRAAMTI 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 337 AEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKvkclggpERNGSVTIVGAV--S 414
Cdd:PRK05922 239 AEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN-------NDKGSITALYAIlhY 311
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 976921132 415 PPGGD-FSDPVTSAtlsivqvfwgLDKKL---AQRKHF--PSVNWLISYSKYSTAL 464
Cdd:PRK05922 312 PNHPDiFTDYLKSL----------LDGHFfltPQGKALasPPIDILTSLSRSARQL 357
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
228-459 |
2.28e-16 |
|
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410876 [Multi-domain] Cd Length: 274 Bit Score: 80.30 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 228 PLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVIsqALskysnsDTV----------VYVGCGERGNEMAevlmdfpQLT 297
Cdd:cd01132 52 PLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTAI--AI------DTIinqkgkkvycIYVAIGQKRSTVA-------QIV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 298 MTLpdgREESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGY 377
Cdd:cd01132 117 KTL---EEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAY 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 378 PA---YLAARLasfYERAGKVK-CLGGpernGSVTIVGAVSPPGGDFSDPVTSATLSIV--QVFwgLDKKLAQRKHFPSV 451
Cdd:cd01132 194 PGdvfYLHSRL---LERAAKLSdELGG----GSLTALPIIETQAGDVSAYIPTNVISITdgQIF--LESELFNKGIRPAI 264
|
....*...
gi 976921132 452 NWLISYSK 459
Cdd:cd01132 265 NVGLSVSR 272
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
215-463 |
8.89e-14 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 74.61 E-value: 8.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 215 TPRP-VASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVIsqALSKYSNSDTV----VYVGCGERGNEMAEV 289
Cdd:CHL00059 110 SPAPgIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAV--ATDTILNQKGQnvicVYVAIGQKASSVAQV 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 290 LMDFpqltmtlpdgREESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLA 369
Cdd:CHL00059 188 VTTL----------QERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLR 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 370 EMPADSGYPA---YLAARLasfYERAGKV-KCLGGpernGSVTIVGAVSPPGGDFSDPVTSATLSIV--QVFwgLDKKLA 443
Cdd:CHL00059 258 RPPGREAYPGdvfYLHSRL---LERAAKLsSQLGE----GSMTALPIVETQAGDVSAYIPTNVISITdgQIF--LSADLF 328
|
250 260
....*....|....*....|
gi 976921132 444 QRKHFPSVNWLISYSKYSTA 463
Cdd:CHL00059 329 NAGIRPAINVGISVSRVGSA 348
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
24-85 |
1.53e-13 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 66.03 E-value: 1.53e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 976921132 24 VRKVSGPVVIADGMAGAA--MYELVRVGHDN----LIGEIIRLEGDSATIQVYEETAGLMVNDPVLRT 85
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLpgLLNALEVELVEfgslVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRT 68
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
21-82 |
1.38e-12 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 63.49 E-value: 1.38e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 976921132 21 CGYVRKVSGPVVIADGMAGAAMYELVRVGHDN------LIGEIIRLEGDSATIQVYEETAGLMVNDPV 82
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGDgnnetvLKAEVIGFRGDRAILQLFESTRGLSRGALV 68
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
39-428 |
4.55e-12 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 68.91 E-value: 4.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 39 GAAMYELVRV--GHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILGNIFDGIQRPLKTIAKRS 116
Cdd:PRK02118 22 GVGYGELATVerKDGSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 117 GDVYIPRGVSV-PAldkdilwefqpKKKGEGDLITGGDLYATVFeNSLVEHHialppdamgKITYIAPPGQyslkdtvle 195
Cdd:PRK02118 102 GEPIEIGGPSVnPV-----------KRIVPREMIRTGIPMIDVF-NTLVESQ---------KIPIFSVSGE--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 196 lefqgvkkkftmlqtwpvrtprPVASKLAadtplltgqRVldALfpsvlggtcaipgafgcgktvisQAlskysNSDTVV 275
Cdd:PRK02118 152 ----------------------PYNALLA---------RI--AL-----------------------QA-----EADIII 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 276 YVGCGERGNemaevlmDFPQLTMTLPDGreeSVMKRTTLVANTSNMPVAAREASIYTGITIAEYFR-DMGYNVSMMADST 354
Cdd:PRK02118 171 LGGMGLTFD-------DYLFFKDTFENA---GALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDM 240
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 976921132 355 SRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAgkVKCLGGpernGSVTIVGAVSPPGGDFSDPVTSAT 428
Cdd:PRK02118 241 TNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKA--VDFEDG----GSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
219-466 |
9.00e-12 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 68.53 E-value: 9.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 219 VASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVIS------------QALSKysNSDTVVYVGCGERGNEM 286
Cdd:PTZ00185 163 IVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAvstiinqvrinqQILSK--NAVISIYVSIGQRCSNV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 287 AEVLMDFpqltmtlpdgREESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISG 366
Cdd:PTZ00185 241 ARIHRLL----------RSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISL 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 367 RLAEMPADSGYPA---YLAARLasfYERAGKVKCLGGperNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLA 443
Cdd:PTZ00185 311 LLRRPPGREAYPGdvfYLHSRL---LERAAMLSPGKG---GGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLF 384
|
250 260
....*....|....*....|...
gi 976921132 444 QRKHFPSVNWLISYSKYSTALES 466
Cdd:PTZ00185 385 TGGQRPAVNIGLSVSRVGSSAQN 407
|
|
| F-box_AtGID2-like |
cd22151 |
F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, ... |
645-686 |
9.44e-12 |
|
F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, also called protein SLEEPY 1, is an essential component of the SCF-type E3 ligase complex, SCF(GID2), a complex that positively regulates the gibberellin signaling pathway. Upon gibberellin treatment, the SCF(GID2) complex mediates the ubiquitination and subsequent degradation of DELLA proteins (GAI, RGA and RGL2), some repressors of the gibberellin pathway, leading to the activation of the pathway. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.
Pssm-ID: 438922 Cd Length: 44 Bit Score: 60.41 E-value: 9.44e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 976921132 645 KLPDHLLIEIFIRVPVVEWGLVSCVSRQWADLFQQECLWHAA 686
Cdd:cd22151 2 KLPDDLLQEIFKRLDPKSLARAACVCRRWRAAARSESLWENA 43
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
8-408 |
8.64e-09 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 58.92 E-value: 8.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 8 RLTTFEDSEKESECGYVRKVSGPVVIADGMAGAAMYELVRVgHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHK 87
Cdd:PRK09281 15 QIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEF-PGGVYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 88 PLSVELGPGILGNIFDGIQRPLktiakrsgdvyiprgvsvpaldkDilwefqpkkkGEGDLITGgdlyatvfENSLVEhh 167
Cdd:PRK09281 94 ILEVPVGEALLGRVVNPLGQPI-----------------------D----------GKGPIEAT--------ETRPVE-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 168 ialppdamgkitYIAPpgqyslkdtvlelefqGVkkkftmlqtwpvrTPR-PVasklaaDTPLLTGQRVLDALFPSVLGG 246
Cdd:PRK09281 131 ------------RKAP----------------GV-------------IDRkSV------HEPLQTGIKAIDAMIPIGRGQ 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 247 TCAIPGAFGCGKTVIsqALskysnsDTV----------VYVGCGERGNEMAevlmdfpQLTMTLpdgREESVMKRTTLVA 316
Cdd:PRK09281 164 RELIIGDRQTGKTAI--AI------DTIinqkgkdvicIYVAIGQKASTVA-------QVVRKL---EEHGAMEYTIVVA 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976921132 317 NTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREIS-------GRLAempadsgYPA---YLAARLa 386
Cdd:PRK09281 226 ATASDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSlllrrppGREA-------YPGdvfYLHSRL- 297
|
410 420
....*....|....*....|...
gi 976921132 387 sfYERAGKV-KCLGGpernGSVT 408
Cdd:PRK09281 298 --LERAAKLsDELGG----GSLT 314
|
|
| ATP-synt_V_A-type_beta_N |
cd18118 |
V/A-type ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the V1/A1 ... |
24-76 |
1.18e-07 |
|
V/A-type ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the V1/A1 complexes of V/A-type ATP synthases, N-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core, that is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex which forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 349742 [Multi-domain] Cd Length: 72 Bit Score: 49.35 E-value: 1.18e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 976921132 24 VRKVSGPVVIADGMAGAAMYELVRVGHDN---LIGEIIRLEGDSATIQVYEETAGL 76
Cdd:cd18118 5 VSEINGPLVIVEGVKGVKYGEIVEITLPDgevRRGQVLEVSGDKAVVQVFEGTSGL 60
|
|
| F-box-like |
pfam12937 |
F-box-like; This is an F-box-like family. |
643-684 |
3.22e-06 |
|
F-box-like; This is an F-box-like family.
Pssm-ID: 463757 [Multi-domain] Cd Length: 45 Bit Score: 44.78 E-value: 3.22e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 976921132 643 FGKLPDHLLIEIFIRVPVVEWGLVSCVSRQWADLFQQECLWH 684
Cdd:pfam12937 1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWR 42
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
476-530 |
1.23e-05 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 43.97 E-value: 1.23e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 976921132 476 IDIRTKAREVLQREDDLNEIVQLVGKDALAETDKITLETAKLLREdYLAQNAFTP 530
Cdd:cd01429 2 KAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEE-FLQQGQFEP 55
|
|
| F-box |
pfam00646 |
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ... |
645-684 |
1.34e-05 |
|
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; pfam00560 and pfam07723) and the WD repeat (pfam00400). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.
Pssm-ID: 425796 Cd Length: 43 Bit Score: 42.91 E-value: 1.34e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 976921132 645 KLPDHLLIEIFIRVPVVEWGLVSCVSRQWADLFQQECLWH 684
Cdd:pfam00646 3 DLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWK 42
|
|
| F-box_FBXL1 |
cd22114 |
F-box domain found in F-box/LRR-repeat protein 1 (FBXL1) and similar proteins; FBXL1, also ... |
643-683 |
2.97e-04 |
|
F-box domain found in F-box/LRR-repeat protein 1 (FBXL1) and similar proteins; FBXL1, also called S-phase kinase-associated protein 2, cyclin-A/CDK2-associated protein p45, F-box protein Skp2, or p45skp2, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. It specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.
Pssm-ID: 438886 Cd Length: 41 Bit Score: 38.93 E-value: 2.97e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 976921132 643 FGKLPDHLLIEIFIRVPVVEWGLVSCVSRQWADLFQQECLW 683
Cdd:cd22114 1 WDSLPDELLLGIFSCLCLPDLLKVSQVCKRWYRLASDESLW 41
|
|
| F-box_SF |
cd09917 |
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ... |
645-678 |
2.52e-03 |
|
F-box domain superfamily; This short domain is commonly found at the N-terminus of various proteins, and typically co-occurs with one or more other conserved domains or motifs, such as leucine rich repeats, WD40 repeats, kelch, tub, spry, and others. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression. One of the best researched roles of F-box proteins is their participation in SCF (Skp1-Cul1-F-box protein), a multi-protein complex that functions as a ubiquitin E3 ligase, where the role of the F-box protein is to recruit target substrates. Gene families containing the F-box are found greatly expanded in narrow taxonomic lineages, such as flowering plants and nematodes. In this hierarchical classification, many of the subfamilies are named according to their domain architectures.
Pssm-ID: 438852 Cd Length: 35 Bit Score: 36.27 E-value: 2.52e-03
10 20 30
....*....|....*....|....*....|....
gi 976921132 645 KLPDHLLIEIFIRVPVVEWGLVSCVSRQWADLFQ 678
Cdd:cd09917 2 DLPDEILLKILSYLDPRDLLRLSLVCKRWRELAS 35
|
|
| F-box_FBXL21 |
cd22179 |
F-box domain found in F-box/LRR-repeat protein 21 (FBXL21) and similar proteins; FBXL21, also ... |
643-683 |
4.13e-03 |
|
F-box domain found in F-box/LRR-repeat protein 21 (FBXL21) and similar proteins; FBXL21, also called F-box and leucine-rich repeat protein 21, F-box and leucine-rich repeat protein 3B (FBXL3B), or F-box/LRR-repeat protein 3B, is the substrate-recognition component of the SCF(FBXL21) E3 ubiquitin ligase complex that mainly acts in the cytosol and mediates ubiquitination of CRY proteins (CRY1 and CRY2), leading to CRY protein stabilization, and thus, is involved in circadian rhythm function. It regulates the oscillation of the circadian clock through ubiquitination and stabilization of cryptochromes. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.
Pssm-ID: 438950 Cd Length: 43 Bit Score: 36.04 E-value: 4.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 976921132 643 FGKLPDHLLIEIFIRVPVVEWGLVSCVSRQWADLFQQECLW 683
Cdd:cd22179 3 WGNLPHHVVLHIFQYLPLVDRARASSVCRRWNEVFHIPDLW 43
|
|
| FBOX |
smart00256 |
A Receptor for Ubiquitination Targets; |
646-684 |
5.94e-03 |
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A Receptor for Ubiquitination Targets;
Pssm-ID: 197608 Cd Length: 41 Bit Score: 35.11 E-value: 5.94e-03
10 20 30
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gi 976921132 646 LPDHLLIEIFIRVPVVEWGLVSCVSRQWADLFQQECLWH 684
Cdd:smart00256 1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWF 39
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| F-box_FBXL7 |
cd22120 |
F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also ... |
643-683 |
7.58e-03 |
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F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also called F-box and leucine-rich repeat protein 7, or F-box protein FBL6/FBL7, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of Aurora kinase A (AURKA) during mitosis, causing mitotic arrest. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.
Pssm-ID: 438892 Cd Length: 44 Bit Score: 35.05 E-value: 7.58e-03
10 20 30 40
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gi 976921132 643 FGKLPDHLLIEIFIRVPVVEWGLVSCVSRQWADLFQQECLW 683
Cdd:cd22120 1 FDRLPDDVILQIFSHLPTNQLCRCARVCRRWYNLAWDPRLW 41
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| F-box_FBXO6-like |
cd22168 |
F-box domain found in F-box only proteins FBXO6, FBXO44 and similar proteins; This subfamily ... |
646-683 |
8.37e-03 |
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F-box domain found in F-box only proteins FBXO6, FBXO44 and similar proteins; This subfamily includes FBXO6 and FBXO44. FBXO6, also called FBX6, F-box protein that recognizes sugar chains 2 (FBS2), or F-box/G-domain protein 2 (FBG2), is a substrate-recognition component of SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complexes. It is involved in the endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins, by recognizing and binding sugar chains on unfolded glycoproteins that are retro-translocated into the cytosol and promoting their ubiquitination and subsequent degradation. FBXO6 can recognize and bind denatured glycoproteins, which are modified with not only high-mannose but also complex-type oligosaccharides. It also recognizes sulfated glycans. FBXO6 is involved in DNA damage response by specifically recognizing activated CHEK1 (phosphorylated on 'Ser-345'), promoting its ubiquitination and degradation. FBXO44, also called FBXO6A, FBX44, or F-box/G-domain protein 3 (FBG3), is a substrate-recognition component of an SCF-type E3 ubiquitin ligase complex. It interacts with SKP1 and CUL1. FBXO44 mediates BRCA1 ubiquitination and degradation. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.
Pssm-ID: 438939 [Multi-domain] Cd Length: 82 Bit Score: 36.11 E-value: 8.37e-03
10 20 30 40
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gi 976921132 646 LPDHLLIEIFIRVPVveWGLV-SC--VSRQWADLFQQECLW 683
Cdd:cd22168 7 LPEDVLLEILSLVPA--RDLIlSCrlVCSRWRDLVDLPTLW 45
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